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Biophysical characterization of bioactive peptide amphiphiles
- Date Issued:
- 2000
- Summary:
- In this present work we have examined the biophysical characterization of two peptides. One alpha-helical (SPARC) and the other triple-helical (collagen). We have compared the effect of lipidation on stabilizing of the alpha-helical and triple-helical peptides. For the first peptide, amino acids from the angiogenesis-inducing region of SPARC were incorporated into alpha-helical peptide sequence. A Tyr was placed between the alpha-helical sequence and the peptide to provide a chromophore; Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Tyr-Lys-His-Gly-Lys-NH 2 was the final sequence. For the second peptide, the sequence chosen to mimic the alpha2beta1 integrin binding site in type I collagen was (Gly-Pro-Hyp)4-Gly-Pro-Ala-Gly-Lys-Asp-Gly-Glu-Ala-Gly-Ala-Gln-(Gly-Pro-Hyp) 4-NH2. Next, each peptide was lipidated with a C-16 acid and was biophysically characterized to determine physiological compatibility. Techniques used included circular dichroism spectroscopy, gel electrophoresis, and Fourier transform infrared spectroscopy. Lastly, one of the peptide amphiphiles was examined as a biomaterial modifier.
Title: | Biophysical characterization of bioactive peptide amphiphiles. |
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Name(s): |
Fishel, Ayala Florida Atlantic University, Degree Grantor Fields, Gregg B., Thesis Advisor |
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Type of Resource: | text | |
Genre: | Electronic Thesis Or Dissertation | |
Issuance: | monographic | |
Date Issued: | 2000 | |
Publisher: | Florida Atlantic University | |
Place of Publication: | Boca Raton, Fla. | |
Physical Form: | application/pdf | |
Extent: | 81 p. | |
Language(s): | English | |
Summary: | In this present work we have examined the biophysical characterization of two peptides. One alpha-helical (SPARC) and the other triple-helical (collagen). We have compared the effect of lipidation on stabilizing of the alpha-helical and triple-helical peptides. For the first peptide, amino acids from the angiogenesis-inducing region of SPARC were incorporated into alpha-helical peptide sequence. A Tyr was placed between the alpha-helical sequence and the peptide to provide a chromophore; Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Tyr-Lys-His-Gly-Lys-NH 2 was the final sequence. For the second peptide, the sequence chosen to mimic the alpha2beta1 integrin binding site in type I collagen was (Gly-Pro-Hyp)4-Gly-Pro-Ala-Gly-Lys-Asp-Gly-Glu-Ala-Gly-Ala-Gln-(Gly-Pro-Hyp) 4-NH2. Next, each peptide was lipidated with a C-16 acid and was biophysically characterized to determine physiological compatibility. Techniques used included circular dichroism spectroscopy, gel electrophoresis, and Fourier transform infrared spectroscopy. Lastly, one of the peptide amphiphiles was examined as a biomaterial modifier. | |
Identifier: | 9780599667389 (isbn), 15780 (digitool), FADT15780 (IID), fau:12532 (fedora) | |
Note(s): | Thesis (M.S.)--Florida Atlantic University, 2000. | |
Subject(s): |
Peptides--Synthesis Lipids Bioactive compounds |
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Held by: | Florida Atlantic University Libraries | |
Persistent Link to This Record: | http://purl.flvc.org/fcla/dt/15780 | |
Sublocation: | Digital Library | |
Use and Reproduction: | Copyright © is held by the author with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder. | |
Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
Host Institution: | FAU | |
Is Part of Series: | Florida Atlantic University Digital Library Collections. |